GPCompReports

OPRK

Gene OPRK1 Opioid receptors Peptide receptors UniProt P41145
811
Total Contact Pairs
87
Significant Changes
12.52
Max Increase
-9.41
Max Decrease

Interactive snake plot

GPCRdb-style topology. Click the view buttons to recolor residues by different data layers. Toggle contact links to draw significant residue-residue contacts as arcs. Click loop labels (ICL/ECL) to expand or collapse loop regions.

Color convention: blue = active-favoring, red = inactive-favoring.

ICL1 T88 12.48x48 T88 12.48x48 T K89 12.49x49 K89 12.49x49 K M90 12.50x50 M90 12.50x50 M K91 12.51x51 K91 12.51x51 K ICL1ECL1 S123 23.49x49 S123 23.49x49 S W124 23.50x50 W124 23.50x50 W P125 23.51x51 P125 23.51x51 P F126 23.52x52 F126 23.52x52 F ECL1ICL2 P163 34.50x50 P163 34.50x50 P V164 34.51x51 V164 34.51x51 V K165 34.52x52 K165 34.52x52 K A166 34.53x53 A166 34.53x53 A L167 34.54x54 L167 34.54x54 L D168 34.55x55 D168 34.55x55 D F169 34.56x56 F169 34.56x56 F R170 34.57x57 R170 34.57x57 R ICL2ECL2 G198 G198 G T199 T199 T K200 K200 K V201 V201 V R202 R202 R E203 E203 E D204 D204 D V205 V205 V D206 D206 D V207 V207 V I208 I208 I E209 E209 E C210 45.50x50 C210 45.50x50 C S211 45.51x51 S211 45.51x51 S L212 45.52x52 L212 45.52x52 L Q213 Q213 Q F214 F214 F P215 P215 P D216 D216 D D217 D217 D ECL2ICL3 R257 R257 R L258 L258 L L259 L259 L S260 S260 S G261 G261 G ICL3ECL3 S301 S301 S T302 T302 T S303 S303 S H304 H304 H ECL3N-term M1 M1 M D2 D2 D S3 S3 S P4 P4 P I5 I5 I Q6 Q6 Q I7 I7 I F8 F8 F R9 R9 R G10 G10 G E11 E11 E P12 P12 P G13 G13 G P14 P14 P T15 T15 T C16 C16 C A17 A17 A P18 P18 P S19 S19 S A20 A20 A C21 C21 C L22 L22 L P23 P23 P P24 P24 P N25 N25 N S26 S26 S S27 S27 S A28 A28 A W29 W29 W F30 F30 F P31 P31 P G32 G32 G W33 W33 W A34 A34 A E35 E35 E P36 P36 P D37 D37 D S38 S38 S N39 N39 N G40 G40 G S41 S41 S A42 A42 A G43 G43 G S44 S44 S E45 E45 E D46 D46 D A47 A47 A Q48 Q48 Q L49 L49 L E50 E50 E P51 P51 P A52 A52 A H53 H53 H I54 I54 I S55 S55 S P56 P56 P N-termC-term P347 P347 P L348 L348 L K349 K349 K M350 M350 M R351 R351 R M352 M352 M E353 E353 E R354 R354 R Q355 Q355 Q S356 S356 S T357 T357 T S358 S358 S R359 R359 R V360 V360 V R361 R361 R N362 N362 N T363 T363 T V364 V364 V Q365 Q365 Q D366 D366 D P367 P367 P A368 A368 A Y369 Y369 Y L370 L370 L R371 R371 R D372 D372 D I373 I373 I D374 D374 D G375 G375 G M376 M376 M N377 N377 N K378 K378 K P379 P379 P V380 V380 V C-term A57 1.30x30 A57 1.30x30 A I58 1.31x31 I58 1.31x31 I P59 1.32x32 P59 1.32x32 P V60 1.33x33 V60 1.33x33 V I61 1.34x34 I61 1.34x34 I I62 1.35x35 I62 1.35x35 I T63 1.36x36 T63 1.36x36 T A64 1.37x37 A64 1.37x37 A V65 1.38x38 V65 1.38x38 V Y66 1.39x39 Y66 1.39x39 Y S67 1.40x40 S67 1.40x40 S V68 1.41x41 V68 1.41x41 V V69 1.42x42 V69 1.42x42 V F70 1.43x43 F70 1.43x43 F V71 1.44x44 V71 1.44x44 V V72 1.45x45 V72 1.45x45 V G73 1.46x46 G73 1.46x46 G L74 1.47x47 L74 1.47x47 L V75 1.48x48 V75 1.48x48 V G76 1.49x49 G76 1.49x49 G N77 1.50x50 N77 1.50x50 N S78 1.51x51 S78 1.51x51 S L79 1.52x52 L79 1.52x52 L V80 1.53x53 V80 1.53x53 V M81 1.54x54 M81 1.54x54 M F82 1.55x55 F82 1.55x55 F V83 1.56x56 V83 1.56x56 V I84 1.57x57 I84 1.57x57 I I85 1.58x58 I85 1.58x58 I R86 1.59x59 R86 1.59x59 R Y87 1.60x60 Y87 1.60x60 Y T92 2.37x37 T92 2.37x37 T A93 2.38x38 A93 2.38x38 A T94 2.39x39 T94 2.39x39 T N95 2.40x40 N95 2.40x40 N I96 2.41x41 I96 2.41x41 I Y97 2.42x42 Y97 2.42x42 Y I98 2.43x43 I98 2.43x43 I F99 2.44x44 F99 2.44x44 F N100 2.45x45 N100 2.45x45 N L101 2.46x46 L101 2.46x46 L A102 2.47x47 A102 2.47x47 A L103 2.48x48 L103 2.48x48 L A104 2.49x49 A104 2.49x49 A D105 2.50x50 D105 2.50x50 D A106 2.51x51 A106 2.51x51 A L107 2.52x52 L107 2.52x52 L V108 2.53x53 V108 2.53x53 V T109 2.54x54 T109 2.54x54 T T110 2.55x55 T110 2.55x55 T T111 2.56x56 T111 2.56x56 T M112 2.57x57 M112 2.57x57 M P113 2.58x58 P113 2.58x58 P F114 2.59x59 F114 2.59x59 F Q115 2.60x60 Q115 2.60x60 Q S116 2.61x61 S116 2.61x61 S T117 2.62x62 T117 2.62x62 T V118 2.63x63 V118 2.63x63 V Y119 2.64x64 Y119 2.64x64 Y L120 2.65x65 L120 2.65x65 L M121 2.66x66 M121 2.66x66 M N122 2.67x67 N122 2.67x67 N G127 3.21x21 G127 3.21x21 G D128 3.22x22 D128 3.22x22 D V129 3.23x23 V129 3.23x23 V L130 3.24x24 L130 3.24x24 L C131 3.25x25 C131 3.25x25 C K132 3.26x26 K132 3.26x26 K I133 3.27x27 I133 3.27x27 I V134 3.28x28 V134 3.28x28 V I135 3.29x29 I135 3.29x29 I S136 3.30x30 S136 3.30x30 S I137 3.31x31 I137 3.31x31 I D138 3.32x32 D138 3.32x32 D Y139 3.33x33 Y139 3.33x33 Y Y140 3.34x34 Y140 3.34x34 Y N141 3.35x35 N141 3.35x35 N M142 3.36x36 M142 3.36x36 M F143 3.37x37 F143 3.37x37 F T144 3.38x38 T144 3.38x38 T S145 3.39x39 S145 3.39x39 S I146 3.40x40 I146 3.40x40 I F147 3.41x41 F147 3.41x41 F T148 3.42x42 T148 3.42x42 T L149 3.43x43 L149 3.43x43 L T150 3.44x44 T150 3.44x44 T M151 3.45x45 M151 3.45x45 M M152 3.46x46 M152 3.46x46 M S153 3.47x47 S153 3.47x47 S V154 3.48x48 V154 3.48x48 V D155 3.49x49 D155 3.49x49 D R156 3.50x50 R156 3.50x50 R Y157 3.51x51 Y157 3.51x51 Y I158 3.52x52 I158 3.52x52 I A159 3.53x53 A159 3.53x53 A V160 3.54x54 V160 3.54x54 V C161 3.55x55 C161 3.55x55 C H162 3.56x56 H162 3.56x56 H T171 4.38x38 T171 4.38x38 T P172 4.39x39 P172 4.39x39 P L173 4.40x40 L173 4.40x40 L K174 4.41x41 K174 4.41x41 K A175 4.42x42 A175 4.42x42 A K176 4.43x43 K176 4.43x43 K I177 4.44x44 I177 4.44x44 I I178 4.45x45 I178 4.45x45 I N179 4.46x46 N179 4.46x46 N I180 4.47x47 I180 4.47x47 I C181 4.48x48 C181 4.48x48 C I182 4.49x49 I182 4.49x49 I W183 4.50x50 W183 4.50x50 W L184 4.51x51 L184 4.51x51 L L185 4.52x52 L185 4.52x52 L S186 4.53x53 S186 4.53x53 S S187 4.54x54 S187 4.54x54 S S188 4.55x55 S188 4.55x55 S V189 4.56x56 V189 4.56x56 V G190 4.57x57 G190 4.57x57 G I191 4.58x58 I191 4.58x58 I S192 4.59x59 S192 4.59x59 S A193 4.60x60 A193 4.60x60 A I194 4.61x61 I194 4.61x61 I V195 4.62x62 V195 4.62x62 V L196 4.63x63 L196 4.63x63 L G197 4.64x64 G197 4.64x64 G D218 5.30x31 D218 5.30x31 D Y219 5.31x32 Y219 5.31x32 Y S220 5.32x33 S220 5.32x33 S W221 5.33x34 W221 5.33x34 W W222 5.34x35 W222 5.34x35 W D223 5.35x36 D223 5.35x36 D L224 5.36x37 L224 5.36x37 L F225 5.37x38 F225 5.37x38 F M226 5.38x39 M226 5.38x39 M K227 5.39x40 K227 5.39x40 K I228 5.40x41 I228 5.40x41 I C229 5.41x42 C229 5.41x42 C V230 5.42x43 V230 5.42x43 V F231 5.43x44 F231 5.43x44 F I232 5.44x45 I232 5.44x45 I F233 5.45x46 F233 5.45x46 F A234 5.46x461 A234 5.46x461 A F235 5.47x47 F235 5.47x47 F V236 5.48x48 V236 5.48x48 V I237 5.49x49 I237 5.49x49 I P238 5.50x50 P238 5.50x50 P V239 5.51x51 V239 5.51x51 V L240 5.52x52 L240 5.52x52 L I241 5.53x53 I241 5.53x53 I I242 5.54x54 I242 5.54x54 I I243 5.55x55 I243 5.55x55 I V244 5.56x56 V244 5.56x56 V C245 5.57x57 C245 5.57x57 C Y246 5.58x58 Y246 5.58x58 Y T247 5.59x59 T247 5.59x59 T L248 5.60x60 L248 5.60x60 L M249 5.61x61 M249 5.61x61 M I250 5.62x62 I250 5.62x62 I L251 5.63x63 L251 5.63x63 L R252 5.64x64 R252 5.64x64 R L253 5.65x65 L253 5.65x65 L K254 5.66x66 K254 5.66x66 K S255 5.67x67 S255 5.67x67 S V256 5.68x68 V256 5.68x68 V S262 6.23x23 S262 6.23x23 S R263 6.24x24 R263 6.24x24 R E264 6.25x25 E264 6.25x25 E K265 6.26x26 K265 6.26x26 K D266 6.27x27 D266 6.27x27 D R267 6.28x28 R267 6.28x28 R N268 6.29x29 N268 6.29x29 N L269 6.30x30 L269 6.30x30 L R270 6.31x31 R270 6.31x31 R R271 6.32x32 R271 6.32x32 R I272 6.33x33 I272 6.33x33 I T273 6.34x34 T273 6.34x34 T R274 6.35x35 R274 6.35x35 R L275 6.36x36 L275 6.36x36 L V276 6.37x37 V276 6.37x37 V L277 6.38x38 L277 6.38x38 L V278 6.39x39 V278 6.39x39 V V279 6.40x40 V279 6.40x40 V V280 6.41x41 V280 6.41x41 V A281 6.42x42 A281 6.42x42 A V282 6.43x43 V282 6.43x43 V F283 6.44x44 F283 6.44x44 F V284 6.45x45 V284 6.45x45 V V285 6.46x46 V285 6.46x46 V C286 6.47x47 C286 6.47x47 C W287 6.48x48 W287 6.48x48 W T288 6.49x49 T288 6.49x49 T P289 6.50x50 P289 6.50x50 P I290 6.51x51 I290 6.51x51 I H291 6.52x52 H291 6.52x52 H I292 6.53x53 I292 6.53x53 I F293 6.54x54 F293 6.54x54 F I294 6.55x55 I294 6.55x55 I L295 6.56x56 L295 6.56x56 L V296 6.57x57 V296 6.57x57 V E297 6.58x58 E297 6.58x58 E A298 6.59x59 A298 6.59x59 A L299 6.60x60 L299 6.60x60 L G300 6.61x61 G300 6.61x61 G S305 7.28x27 S305 7.28x27 S T306 7.29x28 T306 7.29x28 T A307 7.30x29 A307 7.30x29 A A308 7.31x30 A308 7.31x30 A L309 7.32x31 L309 7.32x31 L S310 7.33x32 S310 7.33x32 S S311 7.34x33 S311 7.34x33 S Y312 7.35x34 Y312 7.35x34 Y Y313 7.36x35 Y313 7.36x35 Y F314 7.37x36 F314 7.37x36 F C315 7.38x37 C315 7.38x37 C I316 7.39x38 I316 7.39x38 I A317 7.40x39 A317 7.40x39 A L318 7.41x40 L318 7.41x40 L G319 7.42x41 G319 7.42x41 G Y320 7.43x42 Y320 7.43x42 Y T321 7.44x43 T321 7.44x43 T N322 7.45x45 N322 7.45x45 N S323 7.46x46 S323 7.46x46 S S324 7.47x47 S324 7.47x47 S L325 7.48x48 L325 7.48x48 L N326 7.49x49 N326 7.49x49 N P327 7.50x50 P327 7.50x50 P I328 7.51x51 I328 7.51x51 I L329 7.52x52 L329 7.52x52 L Y330 7.53x53 Y330 7.53x53 Y A331 7.54x54 A331 7.54x54 A F332 7.55x55 F332 7.55x55 F L333 7.56x56 L333 7.56x56 L D334 8.47x47 D334 8.47x47 D E335 8.48x48 E335 8.48x48 E N336 8.49x49 N336 8.49x49 N F341 8.54x54 F341 8.54x54 F R342 8.55x55 R342 8.55x55 R D343 8.56x56 D343 8.56x56 D F337 8.50x50 F337 8.50x50 F K338 8.51x51 K338 8.51x51 K R339 8.52x52 R339 8.52x52 R C340 8.53x53 C340 8.53x53 C F344 8.57x57 F344 8.57x57 F C345 8.58x58 C345 8.58x58 C F346 8.59x59 F346 8.59x59 F

Top 100 conformational changes

Residue pairs with the largest RRCS changes between active and inactive states. GPCRdb numbering in parentheses. Highlighted rows exceed the significance threshold.

Rank Residue 1 Residue 2 Active RRCS Inactive RRCS ΔRRCS Magnitude
1 GLN6 ARG202 12.524 0.000 +12.524 HIGH
2 ARG202 ASP204 10.555 0.970 +9.585 HIGH
3 TYR119 (2.64x64) TYR313 (7.36x35) 12.520 3.063 +9.457 HIGH
4 ASP266 (6.27x27) ARG270 (6.31x31) 1.495 10.910 -9.414 HIGH
5 TYR140 (3.34x34) TRP183 (4.50x50) 10.748 2.177 +8.571 HIGH
6 MET90 (12.50x50) ASN95 (2.40x40) 0.035 8.113 -8.078 HIGH
7 ALA331 (7.54x54) PHE337 (8.50x50) 8.084 0.090 +7.994 HIGH
8 TRP33 ILE54 0.000 7.847 -7.847 HIGH
9 PHE30 GLN115 (2.60x60) 0.000 6.923 -6.923 HIGH
10 ARG267 (6.28x28) ARG271 (6.32x32) 0.000 6.869 -6.869 HIGH
11 TYR246 (5.58x58) LEU277 (6.38x38) 0.000 6.866 -6.866 HIGH
12 TYR87 (1.60x60) PHE344 (8.57x57) 6.861 0.000 +6.861 HIGH
13 ARG371 ASP372 6.717 0.000 +6.717 HIGH
14 TRP33 ASN122 (2.67x67) 0.000 6.613 -6.613 HIGH
15 PHE8 VAL207 6.506 0.000 +6.506 HIGH
16 TYR66 (1.39x39) TYR313 (7.36x35) 6.451 0.000 +6.451 HIGH
17 PHE8 ARG202 6.448 0.000 +6.448 HIGH
18 PRO31 TYR313 (7.36x35) 0.000 5.786 -5.786 HIGH
19 TYR140 (3.34x34) SER186 (4.53x53) 8.438 2.654 +5.784 HIGH
20 LEU370 ARG371 5.780 0.000 +5.780 HIGH
21 LEU258 LYS265 (6.26x26) 5.672 0.000 +5.672 HIGH
22 LEU107 (2.52x52) ASN141 (3.35x35) 5.595 0.000 +5.595 HIGH
23 GLU264 (6.25x25) ARG267 (6.28x28) 5.524 0.000 +5.524 HIGH
24 ASP372 ILE373 5.222 0.000 +5.222 HIGH
25 ARG156 (3.50x50) ARG170 (34.57x57) 0.000 5.203 -5.203 HIGH
26 PHE293 (6.54x54) TYR312 (7.35x34) 5.083 10.283 -5.200 HIGH
27 GLN6 HIS304 5.106 0.000 +5.106 HIGH
28 PHE114 (2.59x59) PHE126 (23.52x52) 1.820 6.751 -4.931 MED
29 PHE8 GLU209 4.880 0.000 +4.880 MED
30 ASP155 (3.49x49) ARG156 (3.50x50) 0.000 4.789 -4.789 MED
31 TYR140 (3.34x34) SER187 (4.54x54) 4.183 8.909 -4.726 MED
32 TYR66 (1.39x39) MET112 (2.57x57) 7.830 3.108 +4.721 MED
33 ILE146 (3.40x40) PHE283 (6.44x44) 0.680 5.387 -4.707 MED
34 SER27 TYR219 (5.31x32) 0.000 4.642 -4.642 MED
35 ARG156 (3.50x50) ILE272 (6.33x33) 0.000 4.631 -4.631 MED
36 THR88 (12.48x48) ASN95 (2.40x40) 4.597 0.000 +4.597 MED
37 LEU259 LYS265 (6.26x26) 4.555 0.000 +4.555 MED
38 MET81 (1.54x54) PHE99 (2.44x44) 2.184 6.468 -4.284 MED
39 ALA331 (7.54x54) LYS338 (8.51x51) 0.000 4.258 -4.258 MED
40 PRO327 (7.50x50) PHE332 (7.55x55) 4.214 0.000 +4.214 MED
41 SER26 GLU297 (6.58x58) 0.000 4.201 -4.201 MED
42 ARG156 (3.50x50) TYR246 (5.58x58) 4.180 0.000 +4.180 MED
43 ASP105 (2.50x50) ASN141 (3.35x35) 0.000 4.135 -4.135 MED
44 ARG271 (6.32x32) GLU335 (8.48x48) 4.636 0.574 +4.062 MED
45 PHE231 (5.43x44) LEU295 (6.56x56) 4.043 0.000 +4.043 MED
46 TYR66 (1.39x39) TYR119 (2.64x64) 0.000 3.948 -3.948 MED
47 THR111 (2.56x56) ASP138 (3.32x32) 5.306 1.359 +3.947 MED
48 PHE332 (7.55x55) LYS338 (8.51x51) 3.921 0.000 +3.921 MED
49 LEU309 (7.32x31) TYR313 (7.36x35) 1.981 5.812 -3.831 MED
50 ASP334 (8.47x47) PHE337 (8.50x50) 0.502 4.098 -3.596 MED
51 PHE30 VAL118 (2.63x63) 0.000 3.579 -3.579 MED
52 TYR66 (1.39x39) TYR320 (7.43x42) 0.000 3.519 -3.519 MED
53 LEU149 (3.43x43) TYR330 (7.53x53) 3.476 0.000 +3.476 MED
54 ILE328 (7.51x51) LEU333 (7.56x56) 3.472 0.000 +3.472 MED
55 TYR97 (2.42x42) MET151 (3.45x45) 0.316 3.753 -3.436 MED
56 MET376 ASN377 5.952 2.530 +3.421 MED
57 LEU333 (7.56x56) LYS338 (8.51x51) 3.393 0.000 +3.393 MED
58 ARG9 HIS304 3.352 0.000 +3.352 MED
59 PHE283 (6.44x44) TRP287 (6.48x48) 4.488 7.830 -3.342 MED
60 GLU11 PRO12 0.477 3.770 -3.292 MED
61 PRO31 TYR312 (7.35x34) 0.000 3.163 -3.163 MED
62 ALA331 (7.54x54) PHE341 (8.54x54) 0.000 3.154 -3.154 MED
63 PRO59 (1.32x32) TYR119 (2.64x64) 5.135 2.031 +3.104 MED
64 ARG252 (5.64x64) SER255 (5.67x67) 3.084 0.000 +3.084 MED
65 VAL108 (2.53x53) TYR320 (7.43x42) 3.809 0.734 +3.075 MED
66 THR111 (2.56x56) TYR320 (7.43x42) 3.073 0.000 +3.073 MED
67 ASN25 TYR219 (5.31x32) 0.000 3.071 -3.071 MED
68 ILE54 THR306 (7.29x28) 3.950 0.906 +3.044 MED
69 THR94 ASP155 (3.49x49) 0.000 2.978 -2.978 MED
70 ILE62 SER310 2.966 0.000 +2.966 MED
71 MET249 THR273 0.000 2.961 -2.961 MED
72 THR94 ARG156 (3.50x50) 0.000 2.932 -2.932 MED
73 TYR140 (3.34x34) ASN141 (3.35x35) 2.910 0.000 +2.910 MED
74 TYR246 (5.58x58) VAL276 3.255 6.134 -2.878 MED
75 TYR119 (2.64x64) SER310 2.877 0.000 +2.877 MED
76 ARG156 (3.50x50) TYR330 (7.53x53) 2.852 0.000 +2.852 MED
77 VAL108 (2.53x53) ASN141 (3.35x35) 3.318 6.138 -2.819 MED
78 VAL296 SER301 6.636 3.842 +2.795 MED
79 VAL83 PHE337 (8.50x50) 3.865 1.075 +2.790 MED
80 PHE8 VAL205 2.775 0.000 +2.775 MED
81 TYR369 LEU370 2.730 0.000 +2.730 MED
82 SER27 LEU212 0.000 2.692 -2.692 MED
83 TRP33 TYR313 (7.36x35) 0.000 2.672 -2.672 MED
84 ASP105 (2.50x50) ASN326 5.583 2.914 +2.669 MED
85 SER27 SER211 0.000 2.662 -2.662 MED
86 PHE30 CYS210 0.000 2.639 -2.639 MED
87 SER26 LYS227 0.000 2.592 -2.592 MED
88 VAL118 (2.63x63) TYR313 (7.36x35) 2.555 0.000 +2.555 LOW
89 ILE96 ASN179 1.140 3.672 -2.531 LOW
90 PHE147 LEU185 1.900 4.381 -2.482 LOW
91 ILE84 LYS89 2.480 0.000 +2.480 LOW
92 LEU79 PHE341 (8.54x54) 1.168 3.617 -2.449 LOW
93 ARG9 THR306 (7.29x28) 2.434 0.000 +2.434 LOW
94 LEU253 LEU259 2.423 0.000 +2.423 LOW
95 VAL279 TYR330 (7.53x53) 2.496 0.098 +2.398 LOW
96 ASP204 VAL205 2.561 0.174 +2.387 LOW
97 ASN100 THR148 0.164 2.542 -2.378 LOW
98 ILE7 GLU209 2.373 0.000 +2.373 LOW
99 TYR157 CYS245 4.622 2.254 +2.367 LOW
100 LEU275 TYR330 (7.53x53) 0.000 2.356 -2.356 LOW

Transmembrane domain analysis

Active-favoring residues form stronger contacts in the active state (positive ΔRRCS). Inactive-favoring residues form stronger contacts in the inactive state (negative ΔRRCS). Only residues with |ΔRRCS| ≥ 2.56 are shown (per-receptor significance threshold = max(mean(|Δ|) + σ, 0.2)).

Per-segment summary
Segment Range Active-favoring residues Count Inactive-favoring residues Count
TM1 59-87 87 (6.9), 66 (6.5), 59 (3.1) 3 81 (-4.3) 1
TM2 95-122 119 (9.5), 107 (5.6), 112 (4.7), 111 (3.9), 108 (3.1) 5 95 (-8.1), 115 (-6.9), 122 (-6.6), 114 (-4.9), 99 (-4.3), 105 (-4.1), 118 (-3.6), 97 (-3.4) 8
TM3 138-156 140 (8.6), 141 (5.6), 138 (3.9), 149 (3.5) 4 156 (-5.2), 155 (-4.8), 146 (-4.7), 151 (-3.4) 4
TM4 183-187 183 (8.6), 186 (5.8) 2 187 (-4.7) 1
TM5 219-255 231 (4.0), 252 (3.1), 255 (3.1) 3 246 (-6.9), 219 (-4.6) 2
TM6 264-297 265 (5.7), 264 (5.5), 295 (4.0) 3 266 (-9.4), 270 (-9.4), 267 (-6.9), 271 (-6.9), 277 (-6.9), 293 (-5.2), 283 (-4.7), 272 (-4.6), 297 (-4.2), 287 (-3.3) 10
TM7 306-333 313 (9.5), 331 (8.0), 327 (4.2), 332 (4.2), 330 (3.5), 328 (3.5), 333 (3.5), 306 (3.0) 8 312 (-5.2), 309 (-3.8), 320 (-3.5) 3
Intracellular / Extracellular loops & H8
ICL1 88-90 88 (4.6) 1 90 (-8.1) 1
ICL2 170-170 - 0 170 (-5.2) 1
ICL3 258-259 258 (5.7), 259 (4.6) 2 - 0
ECL1 126-126 - 0 126 (-4.9) 1
ECL2 202-209 202 (12.5), 204 (9.6), 207 (6.5), 209 (4.9) 4 - 0
ECL3 304-304 304 (5.1) 1 - 0
H8 334-344 337 (8.0), 344 (6.9), 335 (4.1) 3 338 (-4.3), 334 (-3.6), 341 (-3.2) 3

Interactive visualizations

ΔRRCS distribution

Active vs inactive comparison

Residue-wise changes

TM domain breakdown

Variants of interest

122 variants mapped to contact positions, sorted by |ΔRRCS| impact.

Position Protein change DNA change Allele freq Het / Hom ΔRRCS AM score Pathogenicity Conservation dbSNP
6 p.Gln6His c.18G>C 7.08e-07 1 / 0 12.52 0.126 BENIGN 0.62
6 p.Gln6Arg c.17A>G 1.84e-05 26 / 0 12.52 - nan - rs1368538821
204 p.Asp204Gly c.611A>G 7.19e-07 1 / 0 9.59 0.078 BENIGN 0.28
204 p.Asp204His c.610G>C 6.87e-06 10 / 0 9.59 - nan - rs200377155
313 p.Tyr313Phe c.938A>T 6.84e-07 1 / 0 9.46 0.177 BENIGN 0.70
119 p.Tyr119Phe c.356A>T 2.05e-06 3 / 0 9.46 0.167 BENIGN 0.95 rs148980561
313 p.Tyr313Asp c.937T>G 1.37e-06 2 / 0 9.46 - nan - rs1806798924
266 p.Asp266Gly c.797A>G 6.84e-07 1 / 0 9.41 0.938 PATHOGENIC 1.00
270 p.Arg270His c.809G>A 1.16e-05 17 / 0 9.41 0.433 AMBIGUOUS 1.00 rs749949592
270 p.Arg270Pro c.809G>C 2.74e-06 4 / 0 9.41 - nan - rs749949592
270 p.Arg270Cys c.808C>T 7.52e-06 11 / 0 9.41 - nan - rs141228759
266 p.Asp266His c.796G>C 6.84e-07 1 / 0 9.41 - nan -
331 p.Ala331Thr c.991G>A 1.71e-05 25 / 0 7.99 0.824 PATHOGENIC 0.89 rs200397918
331 p.Ala331Ser c.991G>T 6.84e-07 1 / 0 7.99 - nan - rs200397918
33 p.Trp33Cys c.99G>T 6.86e-07 1 / 0 7.85 0.531 AMBIGUOUS 0.36 rs549074768
54 p.Ile54Asn c.161T>A 8.90e-06 13 / 0 7.85 0.386 AMBIGUOUS 0.53 rs776043300
54 p.Ile54Val c.160A>G 2.74e-06 4 / 0 7.85 - nan - rs367824593
33 p.Trp33Cys c.99G>C 6.86e-07 1 / 0 7.85 - nan - rs549074768
30 p.Phe30Leu c.90T>A 2.74e-06 4 / 0 6.92 0.301 BENIGN 0.32 rs1433348238
30 p.Phe30Ile c.88T>A 6.86e-07 1 / 0 6.92 - nan -
30 p.Phe30Leu c.88T>C 6.57e-06 1 / 0 6.92 - nan - rs1807373656
271 p.Arg271Met c.812G>T 6.84e-07 1 / 0 6.87 0.986 PATHOGENIC 1.00
267 p.Arg267His c.800G>A 6.16e-06 9 / 0 6.87 0.339 BENIGN 0.97 rs200420778
267 p.Arg267Leu c.800G>T 1.37e-06 2 / 0 6.87 - nan - rs200420778
267 p.Arg267Cys c.799C>T 7.52e-06 11 / 0 6.87 - nan - rs762806781
267 p.Arg267Ser c.799C>A 1.37e-06 2 / 0 6.87 - nan -
277 p.Leu277Pro c.830T>C 2.74e-06 4 / 0 6.87 0.992 PATHOGENIC 0.93 rs1243582370
246 p.Tyr246Cys c.737A>G 2.74e-06 4 / 0 6.87 0.965 PATHOGENIC 1.00
277 p.Leu277Val c.829C>G 6.84e-07 1 / 0 6.87 - nan -
344 p.Phe344Ile c.1030T>A 6.84e-07 1 / 0 6.86 0.489 AMBIGUOUS 1.00 rs1585626392
371 p.Arg371Ser c.1113G>C 6.84e-07 1 / 0 6.72 0.160 BENIGN 0.61
372 p.Asp372Glu c.1116C>A 2.05e-06 3 / 0 6.72 0.072 BENIGN 0.53
372 p.Asp372Gly c.1115A>G 6.84e-07 1 / 0 6.72 - nan -
372 p.Asp372Tyr c.1114G>T 6.84e-07 1 / 0 6.72 - nan -
372 p.Asp372His c.1114G>C 4.79e-06 7 / 0 6.72 - nan - rs202028631
371 p.Arg371Lys c.1112G>A 4.79e-06 7 / 0 6.72 - nan - rs1806793418
122 p.Asn122Ser c.365A>G 4.10e-06 6 / 0 6.61 0.119 BENIGN 0.57 rs201447402
8 p.Phe8Leu c.24C>G 1.41e-06 2 / 0 6.51 0.765 PATHOGENIC 0.81
207 p.Val207Phe c.619G>T 7.13e-07 1 / 0 6.51 0.171 BENIGN 0.48
8 p.Phe8Leu c.24C>A 7.06e-07 1 / 0 6.51 - nan -
8 p.Phe8Cys c.23T>G 1.31e-05 2 / 0 6.51 - nan - rs908236938
66 p.Tyr66Ser c.197A>C 6.85e-07 1 / 0 6.45 0.952 PATHOGENIC 1.00
66 p.Tyr66Cys c.197A>G 6.85e-07 1 / 0 6.45 - nan -
66 p.Tyr66His c.196T>C 6.84e-07 1 / 0 6.45 - nan -
31 p.Pro31Leu c.92C>T 2.13e-05 31 / 0 5.79 0.103 BENIGN 0.53 rs201985699
31 p.Pro31Ala c.91C>G 6.86e-07 1 / 0 5.79 - nan - rs941657997
31 p.Pro31Ser c.91C>T 1.37e-06 2 / 0 5.79 - nan - rs941657997
186 p.Ser186Leu c.557C>T 8.89e-05 128 / 1 5.78 0.980 PATHOGENIC 0.98 rs143457105
186 p.Ser186Thr c.556T>A 6.84e-07 1 / 0 5.78 - nan -
370 p.Leu370Val c.1108C>G 6.57e-06 1 / 0 5.78 0.055 BENIGN 0.45 rs1806793499
258 p.Leu258Phe c.772C>T 6.84e-07 1 / 0 5.67 0.464 AMBIGUOUS 0.79
107 p.Leu107Phe c.321A>T 6.84e-07 1 / 0 5.59 0.722 PATHOGENIC 0.99
141 p.Asn141Ser c.422A>G 6.84e-07 1 / 0 5.59 0.659 PATHOGENIC 1.00
264 p.Glu264Gly c.791A>G 6.84e-07 1 / 0 5.52 0.697 PATHOGENIC 0.97 rs1563326030
373 p.Ile373Met c.1119C>G 7.53e-06 11 / 0 5.22 0.060 BENIGN 0.65 rs150426309
373 p.Ile373Asn c.1118T>A 6.84e-07 1 / 0 5.22 - nan -
373 p.Ile373Phe c.1117A>T 6.84e-07 1 / 0 5.22 - nan -
373 p.Ile373Val c.1117A>G 3.42e-06 5 / 0 5.22 - nan - rs1411845698
156 p.Arg156His c.467G>A 1.03e-05 15 / 0 5.20 0.994 PATHOGENIC 1.00 rs766490405
170 p.Arg170Leu c.509G>T 6.84e-07 1 / 0 5.20 0.994 PATHOGENIC 0.99 rs894364145
170 p.Arg170His c.509G>A 1.98e-05 29 / 0 5.20 - nan - rs894364145
170 p.Arg170Cys c.508C>T 3.56e-05 52 / 0 5.20 - nan - rs201421010
156 p.Arg156Cys c.466C>T 9.44e-05 138 / 0 5.20 - nan - rs201247710
293 p.Phe293Leu c.879C>A 6.84e-07 1 / 0 5.20 0.984 PATHOGENIC 0.90
293 p.Phe293Cys c.878T>G 6.84e-07 1 / 0 5.20 - nan -
293 p.Phe293Leu c.877T>C 4.10e-06 6 / 0 5.20 - nan - rs764375986
304 p.His304Arg c.911A>G 4.10e-06 6 / 0 5.11 0.070 BENIGN 0.53 rs1806799823
304 p.His304Tyr c.910C>T 4.79e-06 7 / 0 5.11 - nan -
126 p.Phe126Leu c.378T>G 2.74e-06 4 / 0 4.93 0.997 PATHOGENIC 1.00 rs1385730017
126 p.Phe126Ser c.377T>C 6.84e-06 10 / 0 4.93 - nan - rs773135770
155 p.Asp155Asn c.463G>A 2.05e-06 3 / 0 4.79 0.997 PATHOGENIC 1.00
112 p.Met112Thr c.335T>C 6.84e-07 1 / 0 4.72 0.992 PATHOGENIC 0.74 rs753996474
112 p.Met112Val c.334A>G 3.42e-06 5 / 0 4.72 - nan - rs199939072
283 p.Phe283Leu c.847T>C 2.05e-06 3 / 0 4.71 1.000 PATHOGENIC 1.00
27 p.Ser27Arg c.81C>G 1.17e-05 17 / 0 4.64 0.240 BENIGN 0.53 rs766014784
219 p.Tyr219Asp c.655T>G 6.89e-07 1 / 0 4.64 0.214 BENIGN 0.60
27 p.Ser27Asn c.80G>A 6.86e-07 1 / 0 4.64 - nan -
27 p.Ser27Gly c.79A>G 6.86e-07 1 / 0 4.64 - nan -
272 p.Ile272Leu c.814A>C 6.84e-07 1 / 0 4.63 0.878 PATHOGENIC 1.00 rs1329044572
259 p.Leu259Pro c.776T>C 6.57e-06 1 / 0 4.55 0.924 PATHOGENIC 0.97 rs1806804946
99 p.Phe99Leu c.295T>C 6.84e-07 1 / 0 4.28 0.967 PATHOGENIC 0.97
81 p.Met81Ile c.243G>A 2.06e-06 3 / 0 4.28 0.964 PATHOGENIC 0.97 rs1036100225
81 p.Met81Thr c.242T>C 3.43e-06 5 / 0 4.28 - nan -
81 p.Met81Leu c.241A>C 8.23e-06 12 / 0 4.28 - nan - rs1395767420
81 p.Met81Val c.241A>G 6.86e-07 1 / 0 4.28 - nan -
327 p.Pro327Arg c.980C>G 1.37e-06 2 / 0 4.21 0.999 PATHOGENIC 1.00
105 p.Asp105Glu c.315T>A 6.84e-07 1 / 0 4.14 1.000 PATHOGENIC 1.00
105 p.Asp105Asn c.313G>A 6.84e-07 1 / 0 4.14 - nan - rs758708034
231 p.Phe231Leu c.691T>C 9.58e-06 14 / 0 4.04 0.983 PATHOGENIC 1.00 rs956739608
111 p.Thr111Ile c.332C>T 6.84e-07 1 / 0 3.95 0.981 PATHOGENIC 0.98 rs1452068387
111 p.Thr111Ala c.331A>G 6.84e-07 1 / 0 3.95 - nan -
309 p.Leu309Pro c.926T>C 6.84e-07 1 / 0 3.83 0.861 PATHOGENIC 0.53
118 p.Val118Phe c.352G>T 6.84e-07 1 / 0 3.58 0.398 AMBIGUOUS 0.46
320 p.Tyr320Cys c.959A>G 4.10e-06 6 / 0 3.52 0.986 PATHOGENIC 1.00 rs1422323074
330 p.Tyr330Cys c.989A>G 4.10e-06 6 / 0 3.48 0.993 PATHOGENIC 1.00 rs1471140960
333 p.Leu333Pro c.998T>C 3.42e-06 5 / 0 3.47 0.996 PATHOGENIC 0.98 rs756773551
328 p.Ile328Thr c.983T>C 6.84e-07 1 / 0 3.47 0.959 PATHOGENIC 0.77
377 p.Asn377Ser c.1130A>G 6.84e-07 1 / 0 3.42 0.072 BENIGN 0.93
376 p.Met376Thr c.1127T>C 6.84e-06 10 / 0 3.42 0.059 BENIGN 0.61 rs758599432
376 p.Met376Val c.1126A>G 6.84e-07 1 / 0 3.42 - nan -
9 p.Arg9His c.26G>A 2.68e-05 38 / 0 3.35 0.129 BENIGN 0.78 rs762364309
9 p.Arg9Cys c.25C>T 2.82e-06 4 / 0 3.35 - nan - rs770266068
287 p.Trp287Cys c.861G>T 3.42e-06 5 / 0 3.34 0.999 PATHOGENIC 1.00 rs757975302
12 p.Pro12Leu c.35C>T 1.20e-05 17 / 0 3.29 0.089 BENIGN 0.47 rs1007918697
11 p.Glu11Asp c.33G>C 5.63e-06 8 / 0 3.29 0.066 BENIGN 0.68
12 p.Pro12Thr c.34C>A 7.04e-07 1 / 0 3.29 - nan -
12 p.Pro12Ser c.34C>T 7.04e-07 1 / 0 3.29 - nan -
11 p.Glu11Lys c.31G>A 3.52e-06 5 / 0 3.29 - nan -
341 p.Phe341Val c.1021T>G 6.84e-07 1 / 0 3.15 0.835 PATHOGENIC 0.99
59 p.Pro59Leu c.176C>T 4.11e-06 6 / 0 3.10 0.606 PATHOGENIC 0.59 rs1807366599
59 p.Pro59Arg c.176C>G 2.05e-06 3 / 0 3.10 - nan -
59 p.Pro59Ala c.175C>G 6.84e-07 1 / 0 3.10 - nan - rs1334272052
252 p.Arg252Pro c.755G>C 2.05e-06 3 / 0 3.08 0.997 PATHOGENIC 1.00
255 p.Ser255Arg c.765C>A 6.84e-07 1 / 0 3.08 0.667 PATHOGENIC 0.94
252 p.Arg252His c.755G>A 1.03e-05 15 / 0 3.08 - nan - rs200672427
252 p.Arg252Cys c.754C>T 3.42e-06 5 / 0 3.08 - nan - rs772138918
108 p.Val108Ala c.323T>C 2.05e-06 3 / 0 3.08 0.725 PATHOGENIC 0.71 rs765512539
108 p.Val108Ile c.322G>A 6.84e-07 1 / 0 3.08 - nan -
25 p.Asn25Lys c.75C>A 2.75e-06 4 / 0 3.07 0.137 BENIGN 0.56 rs751224173
25 p.Asn25Ser c.74A>G 6.87e-06 10 / 0 3.07 - nan - rs998755241
25 p.Asn25Asp c.73A>G 3.44e-06 5 / 0 3.07 - nan - rs1032860252
306 p.Thr306Pro c.916A>C 5.75e-05 84 / 0 3.04 0.082 BENIGN 0.69 rs199586709

Complete RRCS results

Top 1000 contact pairs by |ΔRRCS|. Significance threshold: |ΔRRCS| ≥ 2.56, computed as max(mean(|Δ|) + σ, 0.2). Highlighted rows indicate significant changes.

Res1 AA1 Res2 AA2 Active RRCS Inactive RRCS ΔRRCS |ΔRRCS|
6 GLN 202 ARG 12.524 0.000 12.524 12.524
202 ARG 204 ASP 10.555 0.970 9.585 9.585
119 TYR 313 TYR 12.520 3.063 9.457 9.457
266 ASP 270 ARG 1.495 10.910 -9.414 9.414
140 TYR 183 TRP 10.748 2.177 8.571 8.571
90 MET 95 ASN 0.035 8.113 -8.078 8.078
331 ALA 337 PHE 8.084 0.090 7.994 7.994
33 TRP 54 ILE 0.000 7.847 -7.847 7.847
30 PHE 115 GLN 0.000 6.923 -6.923 6.923
267 ARG 271 ARG 0.000 6.869 -6.869 6.869
246 TYR 277 LEU 0.000 6.866 -6.866 6.866
87 TYR 344 PHE 6.861 0.000 6.861 6.861
371 ARG 372 ASP 6.717 0.000 6.717 6.717
33 TRP 122 ASN 0.000 6.613 -6.613 6.613
8 PHE 207 VAL 6.506 0.000 6.506 6.506
66 TYR 313 TYR 6.451 0.000 6.451 6.451
8 PHE 202 ARG 6.448 0.000 6.448 6.448
31 PRO 313 TYR 0.000 5.786 -5.786 5.786
140 TYR 186 SER 8.438 2.654 5.784 5.784
370 LEU 371 ARG 5.780 0.000 5.780 5.780
258 LEU 265 LYS 5.672 0.000 5.672 5.672
107 LEU 141 ASN 5.595 0.000 5.595 5.595
264 GLU 267 ARG 5.524 0.000 5.524 5.524
372 ASP 373 ILE 5.222 0.000 5.222 5.222
156 ARG 170 ARG 0.000 5.203 -5.203 5.203
293 PHE 312 TYR 5.083 10.283 -5.200 5.200
6 GLN 304 HIS 5.106 0.000 5.106 5.106
114 PHE 126 PHE 1.820 6.751 -4.931 4.931
8 PHE 209 GLU 4.880 0.000 4.880 4.880
155 ASP 156 ARG 0.000 4.789 -4.789 4.789
140 TYR 187 SER 4.183 8.909 -4.726 4.726
66 TYR 112 MET 7.830 3.108 4.721 4.721
146 ILE 283 PHE 0.680 5.387 -4.707 4.707
27 SER 219 TYR 0.000 4.642 -4.642 4.642
156 ARG 272 ILE 0.000 4.631 -4.631 4.631
88 THR 95 ASN 4.597 0.000 4.597 4.597
259 LEU 265 LYS 4.555 0.000 4.555 4.555
81 MET 99 PHE 2.184 6.468 -4.284 4.284
331 ALA 338 LYS 0.000 4.258 -4.258 4.258
327 PRO 332 PHE 4.214 0.000 4.214 4.214
26 SER 297 GLU 0.000 4.201 -4.201 4.201
156 ARG 246 TYR 4.180 0.000 4.180 4.180
105 ASP 141 ASN 0.000 4.135 -4.135 4.135
271 ARG 335 GLU 4.636 0.574 4.062 4.062
231 PHE 295 LEU 4.043 0.000 4.043 4.043
66 TYR 119 TYR 0.000 3.948 -3.948 3.948
111 THR 138 ASP 5.306 1.359 3.947 3.947
332 PHE 338 LYS 3.921 0.000 3.921 3.921
309 LEU 313 TYR 1.981 5.812 -3.831 3.831
334 ASP 337 PHE 0.502 4.098 -3.596 3.596
30 PHE 118 VAL 0.000 3.579 -3.579 3.579
66 TYR 320 TYR 0.000 3.519 -3.519 3.519
149 LEU 330 TYR 3.476 0.000 3.476 3.476
328 ILE 333 LEU 3.472 0.000 3.472 3.472
97 TYR 151 MET 0.316 3.753 -3.436 3.436
376 MET 377 ASN 5.952 2.530 3.421 3.421
333 LEU 338 LYS 3.393 0.000 3.393 3.393
9 ARG 304 HIS 3.352 0.000 3.352 3.352
283 PHE 287 TRP 4.488 7.830 -3.342 3.342
11 GLU 12 PRO 0.477 3.770 -3.292 3.292
31 PRO 312 TYR 0.000 3.163 -3.163 3.163
331 ALA 341 PHE 0.000 3.154 -3.154 3.154
59 PRO 119 TYR 5.135 2.031 3.104 3.104
252 ARG 255 SER 3.084 0.000 3.084 3.084
108 VAL 320 TYR 3.809 0.734 3.075 3.075
111 THR 320 TYR 3.073 0.000 3.073 3.073
25 ASN 219 TYR 0.000 3.071 -3.071 3.071
54 ILE 306 THR 3.950 0.906 3.044 3.044
94 THR 155 ASP 0.000 2.978 -2.978 2.978
62 ILE 310 SER 2.966 0.000 2.966 2.966
249 MET 273 THR 0.000 2.961 -2.961 2.961
94 THR 156 ARG 0.000 2.932 -2.932 2.932
140 TYR 141 ASN 2.910 0.000 2.910 2.910
246 TYR 276 VAL 3.255 6.134 -2.878 2.878
119 TYR 310 SER 2.877 0.000 2.877 2.877
156 ARG 330 TYR 2.852 0.000 2.852 2.852
108 VAL 141 ASN 3.318 6.138 -2.819 2.819
296 VAL 301 SER 6.636 3.842 2.795 2.795
83 VAL 337 PHE 3.865 1.075 2.790 2.790
8 PHE 205 VAL 2.775 0.000 2.775 2.775
369 TYR 370 LEU 2.730 0.000 2.730 2.730
27 SER 212 LEU 0.000 2.692 -2.692 2.692
33 TRP 313 TYR 0.000 2.672 -2.672 2.672
105 ASP 326 ASN 5.583 2.914 2.669 2.669
27 SER 211 SER 0.000 2.662 -2.662 2.662
30 PHE 210 CYS 0.000 2.639 -2.639 2.639
26 SER 227 LYS 0.000 2.592 -2.592 2.592
118 VAL 313 TYR 2.555 0.000 2.555 2.555
96 ILE 179 ASN 1.140 3.672 -2.531 2.531
147 PHE 185 LEU 1.900 4.381 -2.482 2.482
84 ILE 89 LYS 2.480 0.000 2.480 2.480
79 LEU 341 PHE 1.168 3.617 -2.449 2.449
9 ARG 306 THR 2.434 0.000 2.434 2.434
253 LEU 259 LEU 2.423 0.000 2.423 2.423
279 VAL 330 TYR 2.496 0.098 2.398 2.398
204 ASP 205 VAL 2.561 0.174 2.387 2.387
100 ASN 148 THR 0.164 2.542 -2.378 2.378
7 ILE 209 GLU 2.373 0.000 2.373 2.373
157 TYR 245 CYS 4.622 2.254 2.367 2.367
275 LEU 330 TYR 0.000 2.356 -2.356 2.356
77 ASN 106 ALA 4.010 1.676 2.334 2.334
90 MET 337 PHE 0.000 2.325 -2.325 2.325
214 PHE 219 TYR 7.147 4.862 2.285 2.285
98 ILE 330 TYR 0.940 3.191 -2.251 2.251
115 GLN 313 TYR 2.248 0.000 2.248 2.248
250 ILE 273 THR 2.232 0.000 2.232 2.232
149 LEU 326 ASN 2.205 0.000 2.205 2.205
8 PHE 122 ASN 2.201 0.000 2.201 2.201
330 TYR 337 PHE 0.000 2.183 -2.183 2.183
287 TRP 322 ASN 4.331 2.156 2.175 2.175
139 TYR 193 ALA 0.000 2.155 -2.155 2.155
160 VAL 269 LEU 0.000 2.141 -2.141 2.141
322 ASN 326 ASN 2.201 0.067 2.134 2.134
341 PHE 345 CYS 2.122 0.000 2.122 2.122
140 TYR 190 GLY 0.753 2.870 -2.116 2.116
259 LEU 266 ASP 2.109 0.000 2.109 2.109
89 LYS 95 ASN 2.089 0.000 2.089 2.089
128 ASP 132 LYS 3.753 5.805 -2.052 2.052
202 ARG 209 GLU 0.664 2.689 -2.024 2.024
152 MET 330 TYR 2.107 0.100 2.007 2.007
293 PHE 311 SER 2.004 0.000 2.004 2.004
214 PHE 222 TRP 2.130 4.128 -1.998 1.998
86 ARG 87 TYR 2.720 0.725 1.995 1.995
114 PHE 134 VAL 2.600 0.609 1.991 1.991
105 ASP 145 SER 3.291 1.311 1.979 1.979
77 ASN 105 ASP 5.382 3.404 1.978 1.978
246 TYR 273 THR 0.000 1.949 -1.949 1.949
169 PHE 174 LYS 4.812 2.864 1.947 1.947
142 MET 291 HIS 0.000 1.917 -1.917 1.917
141 ASN 145 SER 0.000 1.908 -1.908 1.908
66 TYR 317 ALA 3.441 1.536 1.906 1.906
365 GLN 366 ASP 1.877 0.000 1.877 1.877
136 SER 140 TYR 0.000 1.872 -1.872 1.872
54 ILE 307 ALA 1.836 0.000 1.836 1.836
114 PHE 130 LEU 1.430 3.248 -1.818 1.818
28 ALA 211 SER 0.000 1.813 -1.813 1.813
79 LEU 344 PHE 0.055 1.861 -1.806 1.806
108 VAL 137 ILE 0.000 1.799 -1.799 1.799
115 GLN 134 VAL 0.000 1.792 -1.792 1.792
29 TRP 139 TYR 0.000 1.788 -1.788 1.788
63 THR 116 SER 0.895 2.677 -1.782 1.782
76 GLY 327 PRO 2.450 4.225 -1.775 1.775
268 ASN 272 ILE 0.000 1.773 -1.773 1.773
62 ILE 313 TYR 0.133 1.906 -1.773 1.773
139 TYR 212 LEU 0.663 2.431 -1.768 1.768
73 GLY 109 THR 0.824 2.588 -1.764 1.764
286 CYS 318 LEU 6.118 7.879 -1.761 1.761
235 PHE 287 TRP 1.736 0.000 1.736 1.736
52 ALA 306 THR 0.000 1.729 -1.729 1.729
143 PHE 189 VAL 2.651 4.369 -1.718 1.718
82 PHE 344 PHE 1.718 0.000 1.718 1.718
96 ILE 175 ALA 0.571 2.279 -1.709 1.709
159 ALA 170 ARG 0.723 2.425 -1.702 1.702
83 VAL 88 THR 1.698 0.000 1.698 1.698
84 ILE 88 THR 1.697 0.000 1.697 1.697
101 LEU 149 LEU 2.276 0.611 1.665 1.665
4 PRO 5 ILE 0.000 1.665 -1.665 1.665
69 VAL 112 MET 2.615 0.952 1.663 1.663
283 PHE 322 ASN 2.272 3.916 -1.645 1.645
136 SER 190 GLY 3.446 1.805 1.641 1.641
25 ASN 209 GLU 0.000 1.640 -1.640 1.640
124 TRP 130 LEU 1.671 3.301 -1.629 1.629
83 VAL 340 CYS 0.000 1.601 -1.601 1.601
290 ILE 315 CYS 3.888 5.482 -1.594 1.594
286 CYS 322 ASN 3.084 1.496 1.587 1.587
97 TYR 175 ALA 2.025 3.592 -1.567 1.567
151 MET 169 PHE 0.095 1.648 -1.553 1.553
368 ALA 369 TYR 1.533 0.000 1.533 1.533
74 LEU 109 THR 1.344 2.876 -1.532 1.532
242 ILE 280 VAL 0.570 2.092 -1.522 1.522
287 TRP 291 HIS 2.147 0.626 1.522 1.522
149 LEU 283 PHE 0.978 2.480 -1.502 1.502
373 ILE 374 ASP 1.498 0.000 1.498 1.498
146 ILE 238 PRO 1.456 2.951 -1.495 1.495
246 TYR 249 MET 1.509 2.998 -1.489 1.489
279 VAL 329 LEU 0.075 1.559 -1.484 1.484
54 ILE 309 LEU 0.000 1.483 -1.483 1.483
90 MET 96 ILE 1.471 0.000 1.471 1.471
140 TYR 144 THR 1.551 0.087 1.465 1.465
117 THR 126 PHE 2.137 3.594 -1.456 1.456
80 VAL 331 ALA 1.447 0.000 1.447 1.447
124 TRP 126 PHE 6.300 4.870 1.430 1.430
72 VAL 324 SER 0.387 1.801 -1.414 1.414
231 PHE 235 PHE 3.148 1.742 1.406 1.406
289 PRO 315 CYS 1.891 3.296 -1.405 1.405
104 ALA 141 ASN 2.907 4.310 -1.403 1.403
146 ILE 287 TRP 1.396 0.000 1.396 1.396
303 SER 305 SER 0.679 2.073 -1.394 1.394
66 TYR 115 GLN 0.633 2.025 -1.392 1.392
27 SER 223 ASP 0.000 1.376 -1.376 1.376
168 ASP 174 LYS 5.698 4.332 1.365 1.365
118 VAL 123 SER 1.737 3.100 -1.363 1.363
140 TYR 191 ILE 0.000 1.345 -1.345 1.345
70 PHE 109 THR 2.270 3.602 -1.332 1.332
136 SER 193 ALA 1.543 0.218 1.324 1.324
155 ASP 170 ARG 8.203 6.888 1.315 1.315
93 ALA 170 ARG 1.189 2.491 -1.302 1.302
142 MET 234 ALA 0.130 1.427 -1.297 1.297
205 VAL 207 VAL 0.539 1.818 -1.279 1.279
314 PHE 318 LEU 1.363 0.085 1.278 1.278
123 SER 208 ILE 4.023 5.298 -1.275 1.275
121 MET 125 PRO 1.266 2.528 -1.262 1.262
22 LEU 23 PRO 1.645 0.391 1.255 1.255
328 ILE 332 PHE 0.118 1.367 -1.249 1.249
239 VAL 283 PHE 1.247 0.000 1.247 1.247
279 VAL 326 ASN 0.000 1.220 -1.220 1.220
108 VAL 142 MET 1.213 0.000 1.213 1.213
100 ASN 144 THR 0.000 1.212 -1.212 1.212
143 PHE 186 SER 2.001 3.206 -1.205 1.205
212 LEU 219 TYR 1.306 0.104 1.201 1.201
149 LEU 279 VAL 0.000 1.200 -1.200 1.200
87 TYR 340 CYS 0.526 1.716 -1.190 1.190
343 ASP 350 MET 0.000 1.185 -1.185 1.185
379 PRO 380 VAL 1.252 0.079 1.173 1.173
84 ILE 90 MET 0.231 1.402 -1.172 1.172
287 TRP 319 GLY 0.336 1.506 -1.170 1.170
161 CYS 252 ARG 1.304 2.471 -1.167 1.167
285 VAL 318 LEU 0.087 1.253 -1.166 1.166
97 TYR 148 THR 1.132 2.295 -1.163 1.163
150 THR 242 ILE 1.295 2.454 -1.160 1.160
5 ILE 297 GLU 1.157 0.000 1.157 1.157
111 THR 137 ILE 0.751 1.908 -1.157 1.157
103 LEU 183 TRP 1.784 0.627 1.157 1.157
290 ILE 312 TYR 1.156 0.000 1.156 1.156
152 MET 276 VAL 0.000 1.155 -1.155 1.155
63 THR 120 LEU 2.624 3.769 -1.145 1.145
62 ILE 66 TYR 1.350 2.491 -1.141 1.141
221 TRP 225 PHE 0.083 1.223 -1.140 1.140
332 PHE 337 PHE 1.139 0.000 1.139 1.139
55 SER 57 ALA 0.000 1.117 -1.117 1.117
44 SER 45 GLU 1.625 0.509 1.116 1.116
137 ILE 141 ASN 1.114 0.000 1.114 1.114
114 PHE 124 TRP 1.976 0.870 1.107 1.107
84 ILE 95 ASN 0.843 1.946 -1.104 1.104
252 ARG 256 VAL 0.784 1.884 -1.101 1.101
128 ASP 199 THR 7.063 5.963 1.099 1.099
97 TYR 179 ASN 4.641 3.543 1.098 1.098
153 SER 245 CYS 2.488 1.391 1.097 1.097
253 LEU 269 LEU 1.083 0.000 1.083 1.083
286 CYS 319 GLY 1.304 2.385 -1.081 1.081
45 GLU 46 ASP 1.079 0.000 1.079 1.079
107 LEU 137 ILE 0.589 1.666 -1.078 1.078
69 VAL 321 THR 2.999 1.931 1.068 1.068
132 LYS 197 GLY 5.649 4.582 1.067 1.067
101 LEU 148 THR 1.791 0.730 1.061 1.061
199 THR 213 GLN 1.560 0.506 1.054 1.054
345 CYS 346 PHE 0.000 1.035 -1.035 1.035
141 ASN 323 SER 0.000 1.029 -1.029 1.029
312 TYR 316 ILE 3.360 4.384 -1.024 1.024
32 GLY 122 ASN 0.000 1.023 -1.023 1.023
29 TRP 316 ILE 0.000 1.020 -1.020 1.020
212 LEU 226 MET 1.018 0.000 1.018 1.018
89 LYS 91 LYS 1.015 0.000 1.015 1.015
142 MET 230 VAL 0.412 1.427 -1.014 1.014
138 ASP 320 TYR 4.118 5.131 -1.013 1.013
142 MET 143 PHE 1.239 0.227 1.012 1.012
264 GLU 268 ASN 1.010 0.000 1.010 1.010
79 LEU 332 PHE 1.009 0.000 1.009 1.009
111 THR 134 VAL 1.201 2.208 -1.007 1.007
66 TYR 316 ILE 2.558 1.555 1.003 1.003
77 ASN 323 SER 1.515 2.500 -0.985 0.985
104 ALA 145 SER 1.374 0.399 0.975 0.975
327 PRO 341 PHE 0.000 0.973 -0.973 0.973
366 ASP 367 PRO 2.642 1.678 0.965 0.965
83 VAL 90 MET 0.000 0.962 -0.962 0.962
69 VAL 324 SER 4.430 5.388 -0.958 0.958
153 SER 276 VAL 0.000 0.955 -0.955 0.955
87 TYR 90 MET 0.000 0.951 -0.951 0.951
119 TYR 316 ILE 0.000 0.942 -0.942 0.942
126 PHE 130 LEU 1.735 2.675 -0.940 0.940
282 VAL 329 LEU 1.406 0.470 0.936 0.936
143 PHE 230 VAL 1.443 0.520 0.922 0.922
290 ILE 319 GLY 0.000 0.922 -0.922 0.922
88 THR 340 CYS 0.913 0.000 0.913 0.913
124 TRP 131 CYS 5.772 6.684 -0.911 0.911
196 LEU 226 MET 0.000 0.905 -0.905 0.905
101 LEU 326 ASN 1.156 2.061 -0.905 0.905
338 LYS 342 ARG 0.000 0.904 -0.904 0.904
290 ILE 316 ILE 1.452 2.353 -0.901 0.901
37 ASP 38 SER 0.899 0.000 0.899 0.899
256 VAL 258 LEU 0.891 0.000 0.891 0.891
282 VAL 325 LEU 0.591 1.478 -0.887 0.887
278 VAL 333 LEU 0.000 0.881 -0.881 0.881
96 ILE 172 PRO 1.986 2.867 -0.880 0.880
160 VAL 252 ARG 2.141 1.261 0.880 0.880
69 VAL 109 THR 0.000 0.877 -0.877 0.877
29 TRP 290 ILE 0.000 0.877 -0.877 0.877
34 ALA 202 ARG 0.000 0.876 -0.876 0.876
100 ASN 183 TRP 3.356 4.232 -0.875 0.875
100 ASN 179 ASN 6.625 7.493 -0.868 0.868
211 SER 213 GLN 0.986 1.850 -0.864 0.864
156 ARG 276 VAL 0.000 0.864 -0.864 0.864
144 THR 183 TRP 1.733 2.594 -0.861 0.861
85 ILE 99 PHE 1.006 1.865 -0.859 0.859
93 ALA 171 THR 0.306 1.164 -0.858 0.858
5 ILE 298 ALA 0.857 0.000 0.857 0.857
101 LEU 105 ASP 2.781 1.934 0.847 0.847
227 LYS 298 ALA 0.843 0.000 0.843 0.843
33 TRP 309 LEU 0.000 0.842 -0.842 0.842
214 PHE 226 MET 1.253 2.087 -0.833 0.833
83 VAL 87 TYR 0.182 1.006 -0.824 0.824
215 PRO 222 TRP 0.000 0.810 -0.810 0.810
332 PHE 341 PHE 0.799 0.000 0.799 0.799
249 MET 276 VAL 0.793 0.000 0.793 0.793
125 PRO 126 PHE 3.885 4.677 -0.792 0.792
96 ILE 100 ASN 0.791 0.000 0.791 0.791
271 ARG 338 LYS 0.791 0.000 0.791 0.791
201 VAL 207 VAL 1.430 2.219 -0.789 0.789
31 PRO 309 LEU 0.000 0.783 -0.783 0.783
101 LEU 145 SER 2.268 3.046 -0.778 0.778
29 TRP 30 PHE 1.067 0.289 0.777 0.777
143 PHE 147 PHE 3.349 2.573 0.776 0.776
29 TRP 119 TYR 0.000 0.775 -0.775 0.775
58 ILE 119 TYR 0.775 0.000 0.775 0.775
111 THR 112 MET 0.000 0.774 -0.774 0.774
151 MET 182 ILE 1.015 0.241 0.774 0.774
158 ILE 166 ALA 1.757 2.527 -0.770 0.770
108 VAL 138 ASP 0.644 1.413 -0.769 0.769
35 GLU 36 PRO 1.546 0.786 0.760 0.760
202 ARG 205 VAL 1.241 2.000 -0.759 0.759
223 ASP 227 LYS 6.800 7.547 -0.747 0.747
278 VAL 329 LEU 0.582 1.324 -0.743 0.743
101 LEU 152 MET 0.773 0.035 0.738 0.738
235 PHE 239 VAL 1.775 1.040 0.735 0.735
329 LEU 330 TYR 0.728 0.000 0.728 0.728
346 PHE 347 PRO 0.824 0.106 0.718 0.718
136 SER 194 ILE 2.923 3.638 -0.716 0.716
200 LYS 213 GLN 4.450 3.737 0.713 0.713
226 MET 230 VAL 0.711 0.000 0.711 0.711
84 ILE 337 PHE 0.205 0.906 -0.702 0.702
144 THR 182 ILE 1.038 1.733 -0.695 0.695
70 PHE 110 THR 0.031 0.725 -0.694 0.694
115 GLN 138 ASP 0.457 1.141 -0.684 0.684
124 TRP 210 CYS 5.476 4.797 0.679 0.679
146 ILE 234 ALA 3.627 2.950 0.678 0.678
326 ASN 330 TYR 1.560 0.883 0.677 0.677
118 VAL 124 TRP 1.210 1.885 -0.675 0.675
72 VAL 328 ILE 0.000 0.670 -0.670 0.670
28 ALA 312 TYR 0.000 0.668 -0.668 0.668
235 PHE 291 HIS 4.142 4.799 -0.657 0.657
132 LYS 195 VAL 0.653 0.000 0.653 0.653
341 PHE 344 PHE 0.652 0.000 0.652 0.652
117 THR 125 PRO 0.000 0.649 -0.649 0.649
166 ALA 170 ARG 0.000 0.649 -0.649 0.649
27 SER 28 ALA 0.649 0.000 0.649 0.649
293 PHE 308 ALA 1.614 2.257 -0.643 0.643
246 TYR 280 VAL 0.914 0.276 0.637 0.637
153 SER 241 ILE 0.634 0.000 0.634 0.634
142 MET 146 ILE 0.631 0.000 0.631 0.631
254 LYS 269 LEU 0.631 0.000 0.631 0.631
77 ASN 102 ALA 6.761 6.130 0.630 0.630
151 MET 154 VAL 0.717 1.347 -0.630 0.630
212 LEU 214 PHE 0.681 1.310 -0.629 0.629
169 PHE 178 ILE 1.531 0.902 0.629 0.629
339 ARG 343 ASP 0.000 0.626 -0.626 0.626
312 TYR 313 TYR 0.871 0.245 0.625 0.625
145 SER 326 ASN 0.624 0.000 0.624 0.624
97 TYR 178 ILE 2.996 3.619 -0.623 0.623
171 THR 174 LYS 2.169 2.789 -0.620 0.620
234 ALA 291 HIS 0.640 0.020 0.620 0.620
80 VAL 330 TYR 0.000 0.616 -0.616 0.616
214 PHE 223 ASP 4.769 5.377 -0.608 0.608
73 GLY 324 SER 4.309 3.703 0.607 0.607
344 PHE 348 LEU 0.595 0.000 0.595 0.595
84 ILE 98 ILE 1.549 0.969 0.580 0.580
235 PHE 288 THR 4.357 4.932 -0.575 0.575
275 LEU 333 LEU 1.214 1.789 -0.575 0.575
30 PHE 31 PRO 0.751 0.180 0.571 0.571
257 ARG 270 ARG 0.000 0.569 -0.569 0.569
356 SER 357 THR 0.565 0.000 0.565 0.565
158 ILE 169 PHE 3.904 3.340 0.564 0.564
108 VAL 323 SER 1.008 1.571 -0.563 0.563
24 PRO 304 HIS 0.000 0.562 -0.562 0.562
313 TYR 316 ILE 0.560 0.000 0.560 0.560
95 ASN 98 ILE 0.000 0.560 -0.560 0.560
153 SER 280 VAL 0.000 0.558 -0.558 0.558
337 PHE 341 PHE 0.429 0.984 -0.556 0.556
85 ILE 91 LYS 0.000 0.551 -0.551 0.551
94 THR 98 ILE 0.695 0.144 0.550 0.550
10 GLY 306 THR 0.550 0.000 0.550 0.550
80 VAL 337 PHE 1.420 1.966 -0.546 0.546
342 ARG 346 PHE 0.000 0.546 -0.546 0.546
105 ASP 323 SER 8.833 8.294 0.539 0.539
58 ILE 313 TYR 0.000 0.539 -0.539 0.539
346 PHE 350 MET 0.539 0.000 0.539 0.539
187 SER 191 ILE 0.041 0.577 -0.535 0.535
94 THR 170 ARG 1.971 1.437 0.534 0.534
223 ASP 226 MET 0.534 0.000 0.534 0.534
7 ILE 202 ARG 0.533 0.000 0.533 0.533
146 ILE 147 PHE 0.074 0.603 -0.529 0.529
70 PHE 113 PRO 1.958 2.485 -0.527 0.527
50 GLU 51 PRO 1.061 0.536 0.525 0.525
119 TYR 120 LEU 0.523 0.000 0.523 0.523
290 ILE 294 ILE 1.307 0.794 0.513 0.513
33 TRP 59 PRO 0.000 0.509 -0.509 0.509
246 TYR 279 VAL 0.503 0.000 0.503 0.503
157 TYR 248 LEU 2.691 3.194 -0.503 0.503
262 SER 265 LYS 0.686 0.184 0.502 0.502
74 LEU 110 THR 0.015 0.515 -0.500 0.500
80 VAL 327 PRO 0.905 0.406 0.499 0.499
124 TRP 134 VAL 0.703 1.195 -0.493 0.493
131 CYS 210 CYS 6.539 7.028 -0.488 0.488
38 SER 39 ASN 0.488 0.000 0.488 0.488
275 LEU 329 LEU 0.265 0.749 -0.484 0.484
249 MET 250 ILE 0.484 0.000 0.484 0.484
153 SER 246 TYR 2.497 2.013 0.484 0.484
335 GLU 338 LYS 1.558 1.077 0.481 0.481
101 LEU 330 TYR 1.201 0.721 0.481 0.481
243 ILE 280 VAL 0.480 0.000 0.480 0.480
70 PHE 112 MET 1.674 1.197 0.477 0.477
25 ASN 26 SER 0.462 0.000 0.462 0.462
148 THR 182 ILE 1.448 1.907 -0.459 0.459
82 PHE 86 ARG 0.000 0.458 -0.458 0.458
218 ASP 222 TRP 1.077 1.530 -0.453 0.453
14 PRO 15 THR 0.000 0.451 -0.451 0.451
286 CYS 321 THR 0.448 0.000 0.448 0.448
123 SER 207 VAL 2.295 1.849 0.446 0.446
93 ALA 175 ALA 1.761 2.205 -0.444 0.444
90 MET 336 ASN 0.000 0.444 -0.444 0.444
260 SER 266 ASP 0.440 0.000 0.440 0.440
132 LYS 194 ILE 2.382 2.820 -0.438 0.438
233 PHE 237 ILE 1.344 0.906 0.438 0.438
28 ALA 210 CYS 0.000 0.431 -0.431 0.431
157 TYR 161 CYS 3.610 3.181 0.429 0.429
303 SER 308 ALA 1.005 1.434 -0.428 0.428
267 ARG 270 ARG 0.537 0.110 0.427 0.427
155 ASP 169 PHE 0.473 0.046 0.426 0.426
115 GLN 320 TYR 1.845 2.268 -0.424 0.424
149 LEU 322 ASN 0.422 0.000 0.422 0.422
145 SER 149 LEU 0.421 0.000 0.421 0.421
143 PHE 234 ALA 1.732 2.149 -0.417 0.417
115 GLN 124 TRP 0.000 0.413 -0.413 0.413
65 VAL 321 THR 0.000 0.409 -0.409 0.409
169 PHE 170 ARG 0.000 0.404 -0.404 0.404
246 TYR 330 TYR 0.402 0.000 0.402 0.402
109 THR 323 SER 0.104 0.505 -0.401 0.401
286 CYS 325 LEU 0.000 0.398 -0.398 0.398
130 LEU 134 VAL 0.701 0.303 0.398 0.398
224 LEU 228 ILE 1.238 1.635 -0.397 0.397
70 PHE 74 LEU 1.024 1.421 -0.396 0.396
344 PHE 345 CYS 0.395 0.000 0.395 0.395
148 THR 179 ASN 0.394 0.000 0.394 0.394
159 ALA 269 LEU 0.000 0.392 -0.392 0.392
237 ILE 241 ILE 0.969 0.580 0.389 0.389
250 ILE 254 LYS 0.476 0.852 -0.376 0.376
29 TRP 312 TYR 0.000 0.375 -0.375 0.375
91 LYS 172 PRO 1.145 0.770 0.375 0.375
153 SER 242 ILE 2.810 2.437 0.373 0.373
146 ILE 242 ILE 0.000 0.372 -0.372 0.372
108 VAL 111 THR 0.000 0.371 -0.371 0.371
231 PHE 236 VAL 5.274 5.642 -0.368 0.368
156 ARG 269 LEU 0.000 0.364 -0.364 0.364
84 ILE 99 PHE 2.774 2.412 0.362 0.362
139 TYR 226 MET 0.359 0.000 0.359 0.359
33 TRP 202 ARG 0.000 0.357 -0.357 0.357
261 GLY 266 ASP 0.355 0.000 0.355 0.355
141 ASN 183 TRP 0.354 0.000 0.354 0.354
122 ASN 207 VAL 2.785 3.132 -0.347 0.347
5 ILE 304 HIS 0.347 0.000 0.347 0.347
29 TRP 287 TRP 0.000 0.346 -0.346 0.346
83 VAL 341 PHE 0.343 0.000 0.343 0.343
98 ILE 334 ASP 0.343 0.000 0.343 0.343
117 THR 121 MET 1.408 1.751 -0.343 0.343
2 ASP 3 SER 0.336 0.000 0.336 0.336
296 VAL 302 THR 1.492 1.828 -0.336 0.336
139 TYR 143 PHE 0.236 0.572 -0.336 0.336
3 SER 4 PRO 0.595 0.931 -0.335 0.335
161 CYS 248 LEU 1.281 0.949 0.332 0.332
135 ILE 211 SER 2.407 2.739 -0.331 0.331
112 MET 317 ALA 0.329 0.000 0.329 0.329
98 ILE 331 ALA 0.328 0.000 0.328 0.328
21 CYS 22 LEU 0.326 0.000 0.326 0.326
153 SER 154 VAL 0.324 0.000 0.324 0.324
146 ILE 150 THR 0.182 0.506 -0.324 0.324
104 ALA 144 THR 1.175 0.852 0.324 0.324
173 LEU 177 ILE 0.771 0.447 0.323 0.323
160 VAL 161 CYS 0.051 0.374 -0.323 0.323
250 ILE 276 VAL 0.322 0.000 0.322 0.322
293 PHE 302 THR 0.010 0.331 -0.321 0.321
103 LEU 107 LEU 0.724 0.405 0.319 0.319
326 ASN 331 ALA 0.318 0.000 0.318 0.318
222 TRP 225 PHE 0.875 0.558 0.317 0.317
131 CYS 198 GLY 2.202 2.517 -0.315 0.315
295 LEU 299 LEU 0.000 0.314 -0.314 0.314
306 THR 310 SER 0.000 0.314 -0.314 0.314
158 ILE 165 LYS 0.038 0.350 -0.312 0.312
366 ASP 368 ALA 0.000 0.311 -0.311 0.311
200 LYS 216 ASP 0.992 0.683 0.309 0.309
156 ARG 273 THR 0.000 0.308 -0.308 0.308
269 LEU 273 THR 0.428 0.121 0.307 0.307
92 THR 94 THR 0.614 0.308 0.306 0.306
253 LEU 272 ILE 0.306 0.000 0.306 0.306
157 TYR 162 HIS 4.424 4.727 -0.303 0.303
289 PRO 318 LEU 0.589 0.288 0.302 0.302
135 ILE 197 GLY 0.099 0.400 -0.302 0.302
100 ASN 182 ILE 0.000 0.301 -0.301 0.301
144 THR 186 SER 5.245 4.945 0.300 0.300
58 ILE 310 SER 1.224 1.522 -0.298 0.298
96 ILE 176 LYS 0.929 1.227 -0.298 0.298
250 ILE 272 ILE 0.297 0.000 0.297 0.297
199 THR 208 ILE 0.908 1.203 -0.295 0.295
238 PRO 283 PHE 0.287 0.000 0.287 0.287
286 CYS 315 CYS 0.132 0.418 -0.286 0.286
79 LEU 82 PHE 0.000 0.284 -0.284 0.284
79 LEU 83 VAL 0.231 0.513 -0.281 0.281
97 TYR 155 ASP 1.016 0.736 0.280 0.280
201 VAL 206 ASP 0.000 0.276 -0.276 0.276
84 ILE 91 LYS 0.000 0.275 -0.275 0.275
143 PHE 233 PHE 0.654 0.928 -0.273 0.273
112 MET 320 TYR 5.594 5.323 0.271 0.271
292 ILE 296 VAL 0.544 0.274 0.270 0.270
198 GLY 213 GLN 3.316 3.583 -0.268 0.268
71 VAL 75 VAL 0.277 0.011 0.265 0.265
151 MET 178 ILE 1.491 1.756 -0.265 0.265
20 ALA 21 CYS 0.264 0.000 0.264 0.264
305 SER 308 ALA 1.049 0.787 0.262 0.262
236 VAL 240 LEU 0.509 0.771 -0.262 0.262
69 VAL 74 LEU 0.000 0.261 -0.261 0.261
139 TYR 230 VAL 0.247 0.508 -0.260 0.260
109 THR 324 SER 0.606 0.347 0.260 0.260
111 THR 115 GLN 0.000 0.259 -0.259 0.259
325 LEU 329 LEU 0.259 0.000 0.259 0.259
196 LEU 212 LEU 2.681 2.939 -0.258 0.258
55 SER 56 PRO 1.211 1.469 -0.258 0.258
6 GLN 204 ASP 0.257 0.000 0.257 0.257
330 TYR 338 LYS 0.000 0.255 -0.255 0.255
28 ALA 30 PHE 0.000 0.253 -0.253 0.253
196 LEU 214 PHE 0.667 0.415 0.252 0.252
156 ARG 159 ALA 0.000 0.249 -0.249 0.249
154 VAL 245 CYS 1.212 1.461 -0.249 0.249
62 ILE 119 TYR 3.965 3.716 0.249 0.249
81 MET 102 ALA 1.177 1.422 -0.245 0.245
329 LEU 334 ASP 0.000 0.245 -0.245 0.245
32 GLY 202 ARG 0.000 0.244 -0.244 0.244
108 VAL 112 MET 0.000 0.242 -0.242 0.242
30 PHE 119 TYR 0.000 0.241 -0.241 0.241
7 ILE 8 PHE 0.000 0.239 -0.239 0.239
299 LEU 301 SER 0.000 0.238 -0.238 0.238
197 GLY 211 SER 1.436 1.673 -0.236 0.236
94 THR 334 ASP 0.235 0.000 0.235 0.235
80 VAL 332 PHE 0.235 0.000 0.235 0.235
128 ASP 198 GLY 2.289 2.056 0.234 0.234
239 VAL 284 VAL 0.226 0.459 -0.232 0.232
132 LYS 193 ALA 0.228 0.000 0.228 0.228
30 PHE 124 TRP 0.000 0.226 -0.226 0.226
150 THR 238 PRO 2.264 2.489 -0.225 0.225
207 VAL 209 GLU 0.000 0.223 -0.223 0.223
255 SER 256 VAL 0.223 0.000 0.223 0.223
25 ASN 27 SER 0.000 0.223 -0.223 0.223
107 LEU 183 TRP 0.154 0.376 -0.222 0.222
74 LEU 106 ALA 0.000 0.221 -0.221 0.221
225 PHE 229 CYS 2.628 2.848 -0.220 0.220
273 THR 277 LEU 0.220 0.000 0.220 0.220
227 LYS 294 ILE 1.758 1.978 -0.219 0.219
271 ARG 333 LEU 0.219 0.000 0.219 0.219
161 CYS 162 HIS 1.200 1.419 -0.218 0.218
219 TYR 223 ASP 0.463 0.245 0.218 0.218
235 PHE 284 VAL 0.003 0.220 -0.217 0.217
124 TRP 208 ILE 6.286 6.503 -0.216 0.216
294 ILE 312 TYR 0.216 0.000 0.216 0.216
78 SER 81 MET 0.065 0.280 -0.215 0.215
185 LEU 188 SER 0.000 0.214 -0.214 0.214
329 LEU 333 LEU 0.186 0.399 -0.214 0.214
116 SER 120 LEU 0.213 0.000 0.213 0.213
147 PHE 233 PHE 1.175 0.962 0.213 0.213
378 LYS 379 PRO 0.076 0.283 -0.207 0.207
200 LYS 209 GLU 6.119 6.325 -0.206 0.206
171 THR 173 LEU 0.265 0.062 0.202 0.202
202 ARG 207 VAL 4.130 3.928 0.202 0.202
154 VAL 241 ILE 0.602 0.400 0.202 0.202
93 ALA 97 TYR 0.201 0.000 0.201 0.201
250 ILE 253 LEU 0.201 0.000 0.201 0.201
188 SER 189 VAL 0.371 0.571 -0.200 0.200
286 CYS 287 TRP 0.080 0.276 -0.196 0.196
139 TYR 190 GLY 0.000 0.195 -0.195 0.195
76 GLY 341 PHE 0.000 0.194 -0.194 0.194
80 VAL 341 PHE 0.000 0.194 -0.194 0.194
254 LYS 260 SER 0.194 0.000 0.194 0.194
81 MET 103 LEU 2.086 2.280 -0.194 0.194
297 GLU 312 TYR 0.193 0.000 0.193 0.193
249 MET 272 ILE 0.192 0.000 0.192 0.192
68 VAL 73 GLY 0.000 0.192 -0.192 0.192
77 ASN 327 PRO 5.385 5.576 -0.191 0.191
149 LEU 152 MET 0.000 0.191 -0.191 0.191
69 VAL 317 ALA 0.190 0.000 0.190 0.190
117 THR 123 SER 0.080 0.267 -0.187 0.187
32 GLY 209 GLU 0.000 0.186 -0.186 0.186
16 CYS 17 ALA 0.000 0.186 -0.186 0.186
232 ILE 237 ILE 5.295 5.481 -0.186 0.186
65 VAL 66 TYR 0.000 0.182 -0.182 0.182
58 ILE 62 ILE 0.730 0.910 -0.180 0.180
112 MET 115 GLN 0.000 0.175 -0.175 0.175
157 TYR 249 MET 0.137 0.309 -0.173 0.173
135 ILE 198 GLY 0.000 0.172 -0.172 0.172
110 THR 111 THR 0.171 0.000 0.171 0.171
94 THR 272 ILE 0.000 0.170 -0.170 0.170
130 LEU 133 ILE 0.000 0.170 -0.170 0.170
198 GLY 211 SER 5.665 5.495 0.169 0.169
305 SER 307 ALA 0.608 0.439 0.168 0.168
139 TYR 142 MET 0.168 0.000 0.168 0.168
58 ILE 59 PRO 1.118 1.285 -0.167 0.167
99 PHE 103 LEU 0.171 0.004 0.167 0.167
184 LEU 187 SER 0.166 0.000 0.166 0.166
7 ILE 297 GLU 0.165 0.000 0.165 0.165
141 ASN 287 TRP 0.000 0.165 -0.165 0.165
33 TRP 58 ILE 0.000 0.164 -0.164 0.164
149 LEU 242 ILE 0.102 0.264 -0.162 0.162
8 PHE 304 HIS 0.162 0.000 0.162 0.162
135 ILE 193 ALA 0.734 0.895 -0.161 0.161
72 VAL 77 ASN 0.000 0.160 -0.160 0.160
74 LEU 78 SER 0.373 0.533 -0.160 0.160
80 VAL 84 ILE 0.743 0.583 0.160 0.160
73 GLY 323 SER 0.000 0.159 -0.159 0.159
17 ALA 18 PRO 0.745 0.586 0.159 0.159
293 PHE 297 GLU 1.035 1.192 -0.157 0.157
87 TYR 343 ASP 0.157 0.000 0.157 0.157
325 LEU 328 ILE 0.311 0.155 0.156 0.156
326 ASN 329 LEU 0.000 0.155 -0.155 0.155
148 THR 152 MET 0.375 0.529 -0.154 0.154
66 TYR 116 SER 3.160 3.314 -0.154 0.154
198 GLY 209 GLU 0.513 0.665 -0.152 0.152
68 VAL 72 VAL 0.305 0.456 -0.151 0.151
54 ILE 58 ILE 1.416 1.266 0.150 0.150
234 ALA 283 PHE 0.322 0.471 -0.150 0.150
230 VAL 235 PHE 0.420 0.569 -0.149 0.149
147 PHE 186 SER 0.678 0.827 -0.149 0.149
152 MET 156 ARG 0.149 0.000 0.149 0.149
160 VAL 273 THR 0.000 0.148 -0.148 0.148
224 LEU 298 ALA 0.690 0.835 -0.145 0.145
248 LEU 251 LEU 0.142 0.000 0.142 0.142
135 ILE 212 LEU 0.880 1.020 -0.139 0.139
160 VAL 249 MET 2.773 2.635 0.139 0.139
334 ASP 335 GLU 0.139 0.000 0.139 0.139
27 SER 214 PHE 0.000 0.137 -0.137 0.137
230 VAL 291 HIS 0.391 0.526 -0.134 0.134
358 SER 359 ARG 0.134 0.000 0.134 0.134
282 VAL 322 ASN 1.048 1.182 -0.134 0.134
63 THR 67 SER 0.103 0.236 -0.132 0.132
144 THR 148 THR 0.280 0.411 -0.131 0.131
98 ILE 337 PHE 0.000 0.129 -0.129 0.129
197 GLY 212 LEU 1.463 1.335 0.128 0.128
192 SER 197 GLY 0.149 0.021 0.128 0.128
249 MET 253 LEU 0.413 0.540 -0.127 0.127
179 ASN 182 ILE 0.290 0.417 -0.127 0.127
241 ILE 245 CYS 0.543 0.417 0.126 0.126
274 ARG 278 VAL 0.000 0.126 -0.126 0.126
77 ASN 326 ASN 0.000 0.124 -0.124 0.124
276 VAL 280 VAL 0.014 0.136 -0.122 0.122
178 ILE 182 ILE 0.416 0.538 -0.122 0.122
284 VAL 288 THR 1.082 1.203 -0.120 0.120
159 ALA 166 ALA 0.911 1.031 -0.120 0.120
73 GLY 78 SER 0.000 0.118 -0.118 0.118
108 VAL 109 THR 0.000 0.118 -0.118 0.118
69 VAL 320 TYR 1.685 1.569 0.116 0.116
122 ASN 309 LEU 0.115 0.000 0.115 0.115
308 ALA 311 SER 0.114 0.000 0.114 0.114
209 GLU 211 SER 0.113 0.000 0.113 0.113
182 ILE 186 SER 0.195 0.308 -0.112 0.112
127 GLY 199 THR 0.761 0.873 -0.111 0.111
262 SER 264 GLU 0.108 0.000 0.108 0.108
278 VAL 282 VAL 0.255 0.149 0.106 0.106
91 LYS 96 ILE 0.000 0.106 -0.106 0.106
225 PHE 226 MET 0.000 0.104 -0.104 0.104
124 TRP 199 THR 1.363 1.466 -0.103 0.103
293 PHE 315 CYS 0.101 0.000 0.101 0.101
229 CYS 234 ALA 0.025 0.126 -0.101 0.101
142 MET 287 TRP 2.948 3.045 -0.097 0.097
77 ASN 109 THR 0.096 0.000 0.096 0.096
187 SER 192 SER 0.000 0.096 -0.096 0.096
26 SER 219 TYR 0.000 0.095 -0.095 0.095
156 ARG 249 MET 1.206 1.300 -0.094 0.094
120 LEU 121 MET 0.000 0.093 -0.093 0.093
135 ILE 210 CYS 1.906 1.817 0.089 0.089
199 THR 209 GLU 3.320 3.231 0.088 0.088
263 ARG 270 ARG 0.340 0.428 -0.088 0.088
332 PHE 333 LEU 0.000 0.088 -0.088 0.088
98 ILE 152 MET 0.576 0.664 -0.088 0.088
275 LEU 279 VAL 0.148 0.060 0.088 0.088
81 MET 106 ALA 0.560 0.474 0.086 0.086
280 VAL 284 VAL 0.227 0.142 0.085 0.085
134 VAL 138 ASP 0.000 0.085 -0.085 0.085
117 THR 122 ASN 0.197 0.112 0.085 0.085
179 ASN 183 TRP 0.084 0.000 0.084 0.084
41 SER 42 ALA 0.000 0.083 -0.083 0.083
233 PHE 238 PRO 2.864 2.947 -0.083 0.083
228 ILE 232 ILE 0.790 0.873 -0.083 0.083
361 ARG 365 GLN 0.000 0.082 -0.082 0.082
110 THR 137 ILE 0.081 0.000 0.081 0.081
151 MET 155 ASP 0.000 0.081 -0.081 0.081
321 THR 325 LEU 1.049 0.969 0.079 0.079
258 LEU 259 LEU 0.000 0.079 -0.079 0.079
105 ASP 327 PRO 0.079 0.000 0.079 0.079
198 GLY 210 CYS 1.062 1.140 -0.077 0.077
232 ILE 238 PRO 0.428 0.505 -0.077 0.077
326 ASN 327 PRO 0.878 0.953 -0.075 0.075
237 ILE 238 PRO 1.334 1.408 -0.075 0.075
28 ALA 29 TRP 0.075 0.000 0.075 0.075
180 ILE 184 LEU 0.605 0.532 0.074 0.074
235 PHE 236 VAL 0.160 0.233 -0.072 0.072
70 PHE 75 VAL 0.000 0.071 -0.071 0.071
290 ILE 291 HIS 0.071 0.000 0.071 0.071
359 ARG 360 VAL 0.069 0.000 0.069 0.069
147 PHE 182 ILE 2.101 2.170 -0.069 0.069
132 LYS 198 GLY 0.809 0.740 0.069 0.069
247 THR 251 LEU 0.406 0.339 0.067 0.067
360 VAL 363 THR 0.000 0.067 -0.067 0.067
231 PHE 232 ILE 0.131 0.065 0.065 0.065
192 SER 196 LEU 0.000 0.065 -0.065 0.065
59 PRO 120 LEU 0.322 0.387 -0.065 0.065
61 ILE 65 VAL 0.008 0.072 -0.065 0.065
115 GLN 316 ILE 0.064 0.000 0.064 0.064
67 SER 116 SER 0.000 0.063 -0.063 0.063
283 PHE 288 THR 0.000 0.063 -0.063 0.063
199 THR 210 CYS 0.091 0.030 0.061 0.061
57 ALA 61 ILE 0.303 0.243 0.060 0.060
53 HIS 306 THR 0.000 0.059 -0.059 0.059
243 ILE 247 THR 0.476 0.417 0.059 0.059
65 VAL 317 ALA 0.352 0.294 0.058 0.058
140 TYR 145 SER 0.000 0.058 -0.058 0.058
201 VAL 208 ILE 0.152 0.210 -0.058 0.058
55 SER 58 ILE 0.000 0.058 -0.058 0.058
358 SER 362 ASN 0.000 0.057 -0.057 0.057
147 PHE 238 PRO 0.000 0.056 -0.056 0.056
80 VAL 98 ILE 0.737 0.792 -0.055 0.055
239 VAL 243 ILE 1.004 0.949 0.055 0.055
196 LEU 211 SER 0.353 0.408 -0.055 0.055
131 CYS 135 ILE 0.908 0.854 0.054 0.054
200 LYS 208 ILE 1.702 1.650 0.051 0.051
162 HIS 165 LYS 0.930 0.980 -0.051 0.051
124 TRP 125 PRO 0.272 0.322 -0.050 0.050
154 VAL 158 ILE 0.805 0.755 0.050 0.050
129 VAL 133 ILE 0.507 0.458 0.049 0.049
70 PHE 71 VAL 0.394 0.345 0.049 0.049
63 THR 119 TYR 0.044 0.093 -0.048 0.048
128 ASP 197 GLY 0.000 0.048 -0.048 0.048
119 TYR 309 LEU 0.047 0.000 0.047 0.047
115 GLN 119 TYR 0.000 0.046 -0.046 0.046
135 ILE 139 TYR 0.968 1.014 -0.046 0.046
71 VAL 76 GLY 0.029 0.074 -0.045 0.045
146 ILE 149 LEU 0.000 0.045 -0.045 0.045
226 MET 227 LYS 0.044 0.000 0.044 0.044
93 ALA 172 PRO 0.030 0.073 -0.043 0.043
288 THR 289 PRO 1.064 1.104 -0.040 0.040
158 ILE 163 PRO 0.612 0.652 -0.040 0.040
272 ILE 276 VAL 0.140 0.180 -0.039 0.039
244 VAL 248 LEU 0.732 0.693 0.039 0.039
137 ILE 138 ASP 0.000 0.038 -0.038 0.038
242 ILE 246 TYR 1.378 1.340 0.038 0.038
160 VAL 253 LEU 1.412 1.374 0.038 0.038
197 GLY 213 GLN 0.032 0.070 -0.037 0.037
65 VAL 69 VAL 0.369 0.332 0.037 0.037
145 SER 283 PHE 0.000 0.036 -0.036 0.036
253 LEU 256 VAL 0.000 0.036 -0.036 0.036
167 LEU 168 ASP 0.000 0.036 -0.036 0.036
230 VAL 234 ALA 0.261 0.226 0.035 0.035
191 ILE 195 VAL 0.081 0.114 -0.033 0.033
99 PHE 100 ASN 0.033 0.000 0.033 0.033
200 LYS 207 VAL 0.585 0.618 -0.033 0.033
94 THR 95 ASN 0.100 0.068 0.033 0.033
15 THR 16 CYS 0.000 0.032 -0.032 0.032
23 PRO 24 PRO 0.826 0.795 0.032 0.032
221 TRP 222 TRP 8.063 8.033 0.031 0.031
171 THR 172 PRO 0.827 0.858 -0.030 0.030
131 CYS 199 THR 1.265 1.296 -0.030 0.030
109 THR 320 TYR 0.030 0.000 0.030 0.030
9 ARG 309 LEU 0.029 0.000 0.029 0.029
150 THR 241 ILE 1.693 1.665 0.028 0.028
193 ALA 212 LEU 1.365 1.392 -0.028 0.028
309 LEU 312 TYR 0.000 0.027 -0.027 0.027
161 CYS 249 MET 0.845 0.870 -0.025 0.025
288 THR 292 ILE 1.218 1.193 0.025 0.025
354 ARG 357 THR 0.000 0.025 -0.025 0.025
90 MET 99 PHE 0.025 0.000 0.025 0.025
231 PHE 291 HIS 2.803 2.828 -0.024 0.024
92 THR 95 ASN 4.160 4.184 -0.024 0.024
139 TYR 189 VAL 0.960 0.936 0.024 0.024
88 THR 91 LYS 0.000 0.024 -0.024 0.024
334 ASP 336 ASN 3.505 3.482 0.023 0.023
242 ILE 283 PHE 0.023 0.000 0.023 0.023
218 ASP 221 TRP 0.000 0.023 -0.023 0.023
282 VAL 286 CYS 0.396 0.418 -0.022 0.022
82 PHE 83 VAL 0.076 0.099 -0.022 0.022
228 ILE 295 LEU 0.022 0.000 0.022 0.022
196 LEU 213 GLN 7.395 7.416 -0.021 0.021
112 MET 113 PRO 0.807 0.787 0.020 0.020
141 ASN 146 ILE 0.000 0.019 -0.019 0.019
297 GLU 302 THR 3.449 3.469 -0.019 0.019
316 ILE 320 TYR 1.655 1.673 -0.019 0.019
284 VAL 289 PRO 0.241 0.223 0.018 0.018
104 ALA 183 TRP 0.000 0.018 -0.018 0.018
302 THR 308 ALA 0.000 0.018 -0.018 0.018
213 GLN 219 TYR 0.017 0.000 0.017 0.017
283 PHE 284 VAL 0.000 0.017 -0.017 0.017
133 ILE 137 ILE 0.882 0.866 0.016 0.016
131 CYS 211 SER 0.450 0.466 -0.016 0.016
157 TYR 158 ILE 0.398 0.383 0.015 0.015
158 ILE 162 HIS 0.107 0.092 0.015 0.015
162 HIS 163 PRO 0.094 0.108 -0.014 0.014
287 TRP 290 ILE 0.468 0.480 -0.013 0.013
97 TYR 152 MET 2.337 2.325 0.012 0.012
80 VAL 102 ALA 0.897 0.885 0.012 0.012
229 CYS 233 PHE 0.112 0.120 -0.008 0.008
124 TRP 209 GLU 0.109 0.102 0.007 0.007
214 PHE 215 PRO 0.874 0.867 0.007 0.007
177 ILE 181 CYS 0.187 0.182 0.005 0.005
253 LEU 257 ARG 0.000 0.004 -0.004 0.004
93 ALA 155 ASP 0.004 0.000 0.004 0.004
77 ASN 101 LEU 0.003 0.000 0.003 0.003
82 PHE 87 TYR 0.003 0.000 0.003 0.003
322 ASN 323 SER 0.000 0.001 -0.001 0.001
91 LYS 92 THR 0.001 0.000 0.001 0.001

RRCS change distribution

-0.01
Mean ΔRRCS
1.84
Std Dev
-0.06
Median

Magnitude classification

27
High (|Δ| ≥ 5.0)
60
Medium (2.6 ≤ |Δ| < 5.0)
724
Low (|Δ| < 2.6)

Methods

RRCS analysis. Residue-Residue Contact Scores (RRCS) were calculated for each conformational state based on inter-atomic distances. Changes (ΔRRCS) were computed by comparing active and inactive structures predicted by AlphaFold multistate (del Alamo et al., 2022).

Significance threshold. |ΔRRCS| ≥ 2.56, computed as max(mean(|Δ|) + σ, 0.2). The 0.2 floor ensures receptors with very small overall change still surface their largest contacts.

Variant data. Population frequencies from gnomAD v4; pathogenicity predictions from AlphaMissense; conservation from ProtVar / UniProt.

Structural annotation. TM domain boundaries and generic numbering from GPCRdb.

What is RRCS?

Residue-Residue Contact Score (RRCS) measures how strongly two amino acids interact in a protein structure. When a protein changes shape (from inactive to active), these contact strengths change.

ΔRRCS (Delta RRCS) shows the difference in contact strength between states:

  • Positive ΔRRCS. Contact is stronger in the active state.
  • Negative ΔRRCS. Contact is stronger in the inactive state.
  • Large |ΔRRCS|. Significant structural rearrangement.

Residues with large RRCS changes are critical for protein function. Mutations at these positions may disrupt the protein's ability to change shape properly.

Pathogenicity predictions

AlphaMissense predicts whether a mutation harms protein function:

  • Pathogenic (score ≥ 0.564): mutation likely damages function.
  • Ambiguous (0.34–0.563): effect uncertain.
  • Benign (< 0.34): mutation likely tolerated.

Conservation & population data

Conservation score. How well-preserved a position is across species (0 = variable, 1 = conserved). High conservation suggests the position is critical for function.

Allele frequency. How often a variant appears in the population. Rare variants (low frequency) may be more likely to be harmful.

Sources: AlphaFold multistate · RRCS · gnomAD v4 · AlphaMissense · GPCRdb · UniProt / ProtVar